Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Bantleon, R.; Altenbuchner, J.; van Pee, K.H.
    Chloroperoxidase from Streptomyces lividans: isolation and characterization of the enzyme and the corresponding gene (1994), J. Bacteriol., 176, 2339-2347.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.B2 3000fold overexpression in Streptomyces aureofaciens Tü24-88 Streptomyces lividans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.1.B2 2.1 2.3 H2O2 bromination of monochlorodimedone Streptomyces lividans
1.11.1.B2 11
-
 Br- bromination of monochlorodimedone Streptomyces lividans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.11.1.B2 additional information enzyme contains no metal Streptomyces lividans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.11.1.B2 32000
-
 2 * 32000, SDS-PAGE Streptomyces lividans
1.11.1.B2 64000
-
 gel filtration Streptomyces lividans

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.B2 Streptomyces lividans
-
 TK64
-
1.11.1.B2 Streptomyces lividans TK64
-
 TK64
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.B2 recombinant enzyme Streptomyces lividans

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.11.1.B2 additional information
-
-
 Streptomyces lividans

Storage Stability

EC Number Storage Stability Organism
1.11.1.B2 -20°C, sodium acetate buffer, pH 5.5, stable for months Streptomyces lividans
1.11.1.B2 6°C, 20 mM sodium acetate buffer, pH 3.5-6, or ammonium acetate buffer, pH 6-8, stable for weeks Streptomyces lividans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.B2 indole + Br- + H2O2
-
 Streptomyces lividans ?
-
 ?
1.11.1.B2 indole + Br- + H2O2
-
 Streptomyces lividans TK64 ?
-
 ?
1.11.1.B2 indole + Cl- + H2O2
-
 Streptomyces lividans oxindole + monochloroindole + H2O
-
 ?
1.11.1.B2 indole + Cl- + H2O2
-
 Streptomyces lividans TK64 oxindole + monochloroindole + H2O
-
 ?
1.11.1.B2 monochlorodimedon + Cl- + H2O2 no activity Streptomyces lividans dichlorodimedon + H2O
-
 ?
1.11.1.B2 monochlorodimedon + Cl- + H2O2 no activity Streptomyces lividans TK64 dichlorodimedon + H2O
-
 ?
1.11.1.B2 monochlorodimedone + Br- + H2O2 all bacterial nonheme haloperoxidases catalyze the bromination, but not the chlorination of monochlorodimedone. Therefore, they are isolated as bromoperoxidases. While the bromination of organic compounds is very unspecific, a substrate specificity exists for the chlorination. Appropriate substrates such as indole or phenyl pyrrole derivatives are chlorinated Streptomyces lividans ?
-
 ?
1.11.1.B2 monochlorodimedone + Br- + H2O2 all bacterial nonheme haloperoxidases catalyze the bromination, but not the chlorination of monochlorodimedone. Therefore, they are isolated as bromoperoxidases. While the bromination of organic compounds is very unspecific, a substrate specificity exists for the chlorination. Appropriate substrates such as indole or phenyl pyrrole derivatives are chlorinated Streptomyces lividans TK64 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.11.1.B2 dimer 2 * 32000, SDS-PAGE Streptomyces lividans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.1.B2 5 5.5 bromination of monochlorodimedone Streptomyces lividans

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.B2 additional information non-heme chloroperoxidase Streptomyces lividans